[ATP-synthase of bacteria, mitochondria, and chloroplasts. Properties of the F(0) membrane sector]

An analysis of literary data concerning the physico-chemical properties of the hydrophobic fragment of bacterial, mitochondrial and chloroplast ATP-synthases has been carried out. The distribution patterns of enzyme subunits and of the whole enzyme complex are reviewed on the basis of amino acid analysis data taking account of physico-chemical characteristics of constituent amino acids. The roles of subunits, their invariant and other amino acids in the hydrophobic fragment function are discussed.